ZN395_HUMAN
ID ZN395_HUMAN Reviewed; 513 AA.
AC Q9H8N7; B3KUY7; D3DST4; Q6F6H2; Q9BY72; Q9NPB2; Q9NS57; Q9NS58; Q9NS59;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Zinc finger protein 395;
DE AltName: Full=HD-regulating factor 2;
DE Short=HDRF-2;
DE AltName: Full=Huntington disease gene regulatory region-binding protein 2;
DE Short=HD gene regulatory region-binding protein 2;
DE Short=HDBP-2;
DE AltName: Full=Papillomavirus regulatory factor 1;
DE Short=PRF-1;
DE AltName: Full=Papillomavirus-binding factor;
GN Name=ZNF395; Synonyms=HDBP2, PBF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, BINDING TO HUMAN
RP PAPILLOMAVIRUS TYPE 8 DNA, AND SUBCELLULAR LOCATION.
RX PubMed=11853404; DOI=10.1006/viro.2001.1231;
RA Boeckle S., Pfister H., Steger G.;
RT "A new cellular factor recognizes E2 binding sites of papillomaviruses
RT which mediate transcriptional repression by E2.";
RL Virology 293:103-117(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DOMAIN, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LEU-109; LEU-113; MET-169 AND MET-172.
RC TISSUE=Testis;
RX PubMed=14625278; DOI=10.1074/jbc.m310726200;
RA Tanaka K., Shouguchi-Miyata J., Miyamoto N., Ikeda J.-E.;
RT "Novel nuclear shuttle proteins, HDBP1 and HDBP2, bind to neuronal cell-
RT specific cis-regulatory element in the promoter for the human Huntington's
RT disease gene.";
RL J. Biol. Chem. 279:7275-7286(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in papillomavirus genes transcription.
CC -!- SUBUNIT: Interacts with repression-mediating E2 binding site P2 of
CC human papillomavirus type 8 (HPV8).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=May shuttle between
CC nucleus and cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11853404,
CC ECO:0000269|PubMed:14625278}.
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DR EMBL; AF263928; AAF73463.1; -; mRNA.
DR EMBL; AB044750; BAA96783.1; -; mRNA.
DR EMBL; AB044751; BAA96784.1; -; mRNA.
DR EMBL; AB044752; BAA96785.1; -; mRNA.
DR EMBL; AB057659; BAB39851.1; -; mRNA.
DR EMBL; AB073627; BAD29734.1; -; mRNA.
DR EMBL; AK002050; BAA92056.1; -; mRNA.
DR EMBL; AK023418; BAB14571.1; -; mRNA.
DR EMBL; AK098243; BAG53599.1; -; mRNA.
DR EMBL; CH471080; EAW63519.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63521.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63522.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63523.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63524.1; -; Genomic_DNA.
DR EMBL; BC001237; AAH01237.1; -; mRNA.
DR CCDS; CCDS6067.1; -.
DR RefSeq; NP_061130.1; NM_018660.2.
DR AlphaFoldDB; Q9H8N7; -.
DR SMR; Q9H8N7; -.
DR BioGRID; 120983; 17.
DR IntAct; Q9H8N7; 7.
DR MINT; Q9H8N7; -.
DR STRING; 9606.ENSP00000340494; -.
DR iPTMnet; Q9H8N7; -.
DR PhosphoSitePlus; Q9H8N7; -.
DR BioMuta; ZNF395; -.
DR DMDM; 84028224; -.
DR EPD; Q9H8N7; -.
DR jPOST; Q9H8N7; -.
DR MassIVE; Q9H8N7; -.
DR MaxQB; Q9H8N7; -.
DR PaxDb; Q9H8N7; -.
DR PeptideAtlas; Q9H8N7; -.
DR PRIDE; Q9H8N7; -.
DR ProteomicsDB; 81230; -.
DR Antibodypedia; 10391; 222 antibodies from 25 providers.
DR DNASU; 55893; -.
DR Ensembl; ENST00000344423.10; ENSP00000340494.5; ENSG00000186918.14.
DR Ensembl; ENST00000523095.5; ENSP00000428452.1; ENSG00000186918.14.
DR Ensembl; ENST00000523202.5; ENSP00000429640.1; ENSG00000186918.14.
DR GeneID; 55893; -.
DR KEGG; hsa:55893; -.
DR MANE-Select; ENST00000344423.10; ENSP00000340494.5; NM_018660.3; NP_061130.1.
DR UCSC; uc003xgq.4; human.
DR CTD; 55893; -.
DR DisGeNET; 55893; -.
DR GeneCards; ZNF395; -.
DR HGNC; HGNC:18737; ZNF395.
DR HPA; ENSG00000186918; Low tissue specificity.
DR MIM; 609494; gene.
DR neXtProt; NX_Q9H8N7; -.
DR OpenTargets; ENSG00000186918; -.
DR PharmGKB; PA134978145; -.
DR VEuPathDB; HostDB:ENSG00000186918; -.
DR eggNOG; ENOG502QW7P; Eukaryota.
DR GeneTree; ENSGT00940000157136; -.
DR HOGENOM; CLU_032989_2_1_1; -.
DR InParanoid; Q9H8N7; -.
DR OMA; NGQECAG; -.
DR OrthoDB; 915379at2759; -.
DR PhylomeDB; Q9H8N7; -.
DR TreeFam; TF326610; -.
DR PathwayCommons; Q9H8N7; -.
DR SignaLink; Q9H8N7; -.
DR BioGRID-ORCS; 55893; 21 hits in 1086 CRISPR screens.
DR ChiTaRS; ZNF395; human.
DR GenomeRNAi; 55893; -.
DR Pharos; Q9H8N7; Tbio.
DR PRO; PR:Q9H8N7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H8N7; protein.
DR Bgee; ENSG00000186918; Expressed in nipple and 201 other tissues.
DR ExpressionAtlas; Q9H8N7; baseline and differential.
DR Genevisible; Q9H8N7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:UniProtKB.
DR InterPro; IPR031940; DUF4772.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF15997; DUF4772; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..513
FT /note="Zinc finger protein 395"
FT /id="PRO_0000047561"
FT ZN_FING 280..305
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 17..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 165..174
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 109
FT /note="L->A: No change in subcellular location; when
FT associated with A-113."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 113
FT /note="L->A: No change in subcellular location; when
FT associated with A-109."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 169
FT /note="M->A: No shuttle from the nucleus to the cytoplasm;
FT when associated with A-172."
FT /evidence="ECO:0000269|PubMed:14625278"
FT MUTAGEN 172
FT /note="M->A: No shuttle from the nucleus to the cytoplasm;
FT when associated with A-169."
FT /evidence="ECO:0000269|PubMed:14625278"
FT CONFLICT 140
FT /note="G -> R (in Ref. 2; BAA96783/BAD29734)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="L -> Q (in Ref. 3; BAB14571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 54939 MW; 992990499E228EB8 CRC64;
MASVLSRRLG KRSLLGARVL GPSASEGPSA APPSEPLLEG AAPQPFTTSD DTPCQEQPKE
VLKAPSTSGL QQVAFQPGQK VYVWYGGQEC TGLVEQHSWM EGQVTVWLLE QKLQVCCRVE
EVWLAELQGP CPQAPPLEPG AQALAYRPVS RNIDVPKRKS DAVEMDEMMA AMVLTSLSCS
PVVQSPPGTE ANFSASRAAC DPWKESGDIS DSGSSTTSGH WSGSSGVSTP SPPHPQASPK
YLGDAFGSPQ TDHGFETDPD PFLLDEPAPR KRKNSVKVMY KCLWPNCGKV LRSIVGIKRH
VKALHLGDTV DSDQFKREED FYYTEVQLKE ESAAAAAAAA AGTPVPGTPT SEPAPTPSMT
GLPLSALPPP LHKAQSSGPE HPGPESSLPS GALSKSAPGS FWHIQADHAY QALPSFQIPV
SPHIYTSVSW AAAPSAACSL SPVRSRSLSF SEPQQPAPAM KSHLIVTSPP RAQSGARKAR
GEAKKCRKVY GIEHRDQWCT ACRWKKACQR FLD
